Membrane-associated DegP in Bordetella chaperones a repeat-rich secretory protein.
Identifieur interne : 002453 ( Main/Exploration ); précédent : 002452; suivant : 002454Membrane-associated DegP in Bordetella chaperones a repeat-rich secretory protein.
Auteurs : Catherine Baud [France] ; Irina Gutsche ; Eve Willery ; Diane De Paepe ; Hervé Drobecq ; Martine Gilleron ; Camille Locht ; Marc Jamin ; Françoise Jacob-DubuissonSource :
- Molecular microbiology [ 1365-2958 ] ; 2011.
Descripteurs français
- KwdFr :
- Bordetella pertussis (), Bordetella pertussis (enzymologie), Bordetella pertussis (génétique), Bordetella pertussis (métabolisme), Chaperons moléculaires (), Chaperons moléculaires (génétique), Chaperons moléculaires (métabolisme), Facteurs de virulence des Bordetella (), Facteurs de virulence des Bordetella (génétique), Facteurs de virulence des Bordetella (métabolisme), Membrane cellulaire (), Membrane cellulaire (enzymologie), Membrane cellulaire (génétique), Membrane cellulaire (métabolisme), Protéines du choc thermique (), Protéines du choc thermique (génétique), Protéines du choc thermique (métabolisme), Protéines périplasmiques (), Protéines périplasmiques (génétique), Protéines périplasmiques (métabolisme), Serine endopeptidases (), Serine endopeptidases (génétique), Serine endopeptidases (métabolisme), Spécificité du substrat, Structure tertiaire des protéines, Transport de protéines.
- MESH :
- enzymologie : Bordetella pertussis, Membrane cellulaire.
- génétique : Bordetella pertussis, Chaperons moléculaires, Facteurs de virulence des Bordetella, Membrane cellulaire, Protéines du choc thermique, Protéines périplasmiques, Serine endopeptidases.
- métabolisme : Bordetella pertussis, Chaperons moléculaires, Facteurs de virulence des Bordetella, Membrane cellulaire, Protéines du choc thermique, Protéines périplasmiques, Serine endopeptidases.
- Bordetella pertussis, Chaperons moléculaires, Facteurs de virulence des Bordetella, Membrane cellulaire, Protéines du choc thermique, Protéines périplasmiques, Serine endopeptidases, Spécificité du substrat, Structure tertiaire des protéines, Transport de protéines.
English descriptors
- KwdEn :
- Bordetella pertussis (chemistry), Bordetella pertussis (enzymology), Bordetella pertussis (genetics), Bordetella pertussis (metabolism), Cell Membrane (chemistry), Cell Membrane (enzymology), Cell Membrane (genetics), Cell Membrane (metabolism), Heat-Shock Proteins (chemistry), Heat-Shock Proteins (genetics), Heat-Shock Proteins (metabolism), Molecular Chaperones (chemistry), Molecular Chaperones (genetics), Molecular Chaperones (metabolism), Periplasmic Proteins (chemistry), Periplasmic Proteins (genetics), Periplasmic Proteins (metabolism), Protein Structure, Tertiary, Protein Transport, Serine Endopeptidases (chemistry), Serine Endopeptidases (genetics), Serine Endopeptidases (metabolism), Substrate Specificity, Virulence Factors, Bordetella (chemistry), Virulence Factors, Bordetella (genetics), Virulence Factors, Bordetella (metabolism).
- MESH :
- chemical , chemistry : Heat-Shock Proteins, Molecular Chaperones, Periplasmic Proteins, Serine Endopeptidases, Virulence Factors, Bordetella.
- chemistry : Bordetella pertussis, Cell Membrane.
- enzymology : Bordetella pertussis, Cell Membrane.
- genetics : Bordetella pertussis, Cell Membrane, Heat-Shock Proteins, Molecular Chaperones, Periplasmic Proteins, Serine Endopeptidases, Virulence Factors, Bordetella.
- metabolism : Bordetella pertussis, Cell Membrane, Heat-Shock Proteins, Molecular Chaperones, Periplasmic Proteins, Serine Endopeptidases, Virulence Factors, Bordetella.
- Protein Structure, Tertiary, Protein Transport, Substrate Specificity.
Abstract
The chaperone/protease DegP belongs to the HtrA superfamily and is involved in protein quality control in the periplasm of Gram-negative bacteria. In Escherichia coli, typical substrates are unfolded or misfolded globular proteins that trigger the rearrangement of inactive DegP hexamers into substrate-sequestering 12- or 24-mers 'cages' for refolding or degradation. In Bordetella pertussis, DegP(Bp) facilitates, in addition, the secretion of FHA, a long β-helical adhesin that passes through the periplasm in an extended conformation. We show that DegP(Bp) exists as soluble trimers and as a membrane-associated form. Different substrates interact differently with the distinct forms of DegP(Bp), and membrane-associated DegP(Bp) has high affinity for non-native FHA. Unlike more globular substrates, FHA does not efficiently mediate rearrangement of trimers into proteolytically active, short-lived dodecamers. In contrast to these dodecamers, membrane-associated DegP(Bp) is not committed to substrate degradation, although it is proteolytically competent. In B. pertussis, membrane-associated DegP(Bp) thus represents a specific functional form serving as a holding chaperone for client proteins including FHA. If FHA secretion is impaired, membrane-associated DegP(Bp) participates in its degradation. This form of DegP(Bp) is appropriate to handle substrates unsuitable to be sequestered in cages or non-folded, secretory proteins that must not be degraded.
DOI: 10.1111/j.1365-2958.2011.07672.x
PubMed: 21518392
Affiliations:
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first="Eve" last="Willery">Eve Willery</name></author><author><name sortKey="De Paepe, Diane" sort="De Paepe, Diane" uniqKey="De Paepe D" first="Diane" last="De Paepe">Diane De Paepe</name></author><author><name sortKey="Drobecq, Herve" sort="Drobecq, Herve" uniqKey="Drobecq H" first="Hervé" last="Drobecq">Hervé Drobecq</name></author><author><name sortKey="Gilleron, Martine" sort="Gilleron, Martine" uniqKey="Gilleron M" first="Martine" last="Gilleron">Martine Gilleron</name></author><author><name sortKey="Locht, Camille" sort="Locht, Camille" uniqKey="Locht C" first="Camille" last="Locht">Camille Locht</name></author><author><name sortKey="Jamin, Marc" sort="Jamin, Marc" uniqKey="Jamin M" first="Marc" last="Jamin">Marc Jamin</name></author><author><name sortKey="Jacob Dubuisson, Francoise" sort="Jacob Dubuisson, Francoise" uniqKey="Jacob Dubuisson F" first="Françoise" last="Jacob-Dubuisson">Françoise Jacob-Dubuisson</name></author></titleStmt><publicationStmt><idno 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xml:lang="en">Membrane-associated DegP in Bordetella chaperones a repeat-rich secretory protein.</title><author><name sortKey="Baud, Catherine" sort="Baud, Catherine" uniqKey="Baud C" first="Catherine" last="Baud">Catherine Baud</name><affiliation wicri:level="3"><nlm:affiliation>Inserm U1019, Center for Infection and Immunity of Lille, F-59019 Lille, France.</nlm:affiliation><country xml:lang="fr">France</country><wicri:regionArea>Inserm U1019, Center for Infection and Immunity of Lille, F-59019 Lille</wicri:regionArea><placeName><region type="region" nuts="2">Hauts-de-France</region><region type="old region" nuts="2">Nord-Pas-de-Calais</region><settlement type="city">Lille</settlement></placeName></affiliation></author><author><name sortKey="Gutsche, Irina" sort="Gutsche, Irina" uniqKey="Gutsche I" first="Irina" last="Gutsche">Irina Gutsche</name></author><author><name sortKey="Willery, Eve" sort="Willery, Eve" uniqKey="Willery E" first="Eve" last="Willery">Eve Willery</name></author><author><name sortKey="De Paepe, Diane" sort="De Paepe, Diane" uniqKey="De Paepe D" first="Diane" last="De Paepe">Diane De Paepe</name></author><author><name sortKey="Drobecq, Herve" sort="Drobecq, Herve" uniqKey="Drobecq H" first="Hervé" last="Drobecq">Hervé Drobecq</name></author><author><name sortKey="Gilleron, Martine" sort="Gilleron, Martine" uniqKey="Gilleron M" first="Martine" last="Gilleron">Martine Gilleron</name></author><author><name sortKey="Locht, Camille" sort="Locht, Camille" uniqKey="Locht C" first="Camille" last="Locht">Camille Locht</name></author><author><name sortKey="Jamin, Marc" sort="Jamin, Marc" uniqKey="Jamin M" first="Marc" last="Jamin">Marc Jamin</name></author><author><name sortKey="Jacob Dubuisson, Francoise" sort="Jacob Dubuisson, Francoise" uniqKey="Jacob Dubuisson F" first="Françoise" last="Jacob-Dubuisson">Françoise Jacob-Dubuisson</name></author></analytic><series><title level="j">Molecular microbiology</title><idno type="eISSN">1365-2958</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bordetella pertussis (chemistry)</term><term>Bordetella pertussis (enzymology)</term><term>Bordetella pertussis (genetics)</term><term>Bordetella pertussis (metabolism)</term><term>Cell Membrane (chemistry)</term><term>Cell Membrane (enzymology)</term><term>Cell Membrane (genetics)</term><term>Cell Membrane (metabolism)</term><term>Heat-Shock Proteins (chemistry)</term><term>Heat-Shock Proteins (genetics)</term><term>Heat-Shock Proteins (metabolism)</term><term>Molecular Chaperones (chemistry)</term><term>Molecular Chaperones (genetics)</term><term>Molecular Chaperones (metabolism)</term><term>Periplasmic Proteins (chemistry)</term><term>Periplasmic Proteins (genetics)</term><term>Periplasmic Proteins (metabolism)</term><term>Protein Structure, Tertiary</term><term>Protein Transport</term><term>Serine Endopeptidases (chemistry)</term><term>Serine Endopeptidases (genetics)</term><term>Serine Endopeptidases (metabolism)</term><term>Substrate Specificity</term><term>Virulence Factors, Bordetella (chemistry)</term><term>Virulence Factors, Bordetella (genetics)</term><term>Virulence Factors, Bordetella (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Bordetella pertussis ()</term><term>Bordetella pertussis (enzymologie)</term><term>Bordetella pertussis (génétique)</term><term>Bordetella pertussis (métabolisme)</term><term>Chaperons moléculaires ()</term><term>Chaperons moléculaires (génétique)</term><term>Chaperons moléculaires (métabolisme)</term><term>Facteurs de virulence des Bordetella ()</term><term>Facteurs de virulence des Bordetella (génétique)</term><term>Facteurs de virulence des Bordetella (métabolisme)</term><term>Membrane cellulaire ()</term><term>Membrane cellulaire (enzymologie)</term><term>Membrane cellulaire (génétique)</term><term>Membrane cellulaire (métabolisme)</term><term>Protéines du choc thermique ()</term><term>Protéines du choc thermique (génétique)</term><term>Protéines du choc thermique (métabolisme)</term><term>Protéines périplasmiques ()</term><term>Protéines périplasmiques (génétique)</term><term>Protéines périplasmiques (métabolisme)</term><term>Serine endopeptidases ()</term><term>Serine endopeptidases (génétique)</term><term>Serine endopeptidases (métabolisme)</term><term>Spécificité du substrat</term><term>Structure tertiaire des protéines</term><term>Transport de protéines</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Heat-Shock Proteins</term><term>Molecular Chaperones</term><term>Periplasmic Proteins</term><term>Serine Endopeptidases</term><term>Virulence Factors, Bordetella</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Bordetella pertussis</term><term>Cell Membrane</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Bordetella pertussis</term><term>Membrane cellulaire</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Bordetella pertussis</term><term>Cell Membrane</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Bordetella pertussis</term><term>Cell Membrane</term><term>Heat-Shock Proteins</term><term>Molecular Chaperones</term><term>Periplasmic Proteins</term><term>Serine Endopeptidases</term><term>Virulence Factors, Bordetella</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Bordetella pertussis</term><term>Chaperons moléculaires</term><term>Facteurs de virulence des Bordetella</term><term>Membrane cellulaire</term><term>Protéines du choc thermique</term><term>Protéines périplasmiques</term><term>Serine endopeptidases</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Bordetella pertussis</term><term>Cell Membrane</term><term>Heat-Shock Proteins</term><term>Molecular Chaperones</term><term>Periplasmic Proteins</term><term>Serine Endopeptidases</term><term>Virulence Factors, Bordetella</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Bordetella pertussis</term><term>Chaperons moléculaires</term><term>Facteurs de virulence des Bordetella</term><term>Membrane cellulaire</term><term>Protéines du choc thermique</term><term>Protéines périplasmiques</term><term>Serine endopeptidases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Protein Structure, Tertiary</term><term>Protein Transport</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Bordetella pertussis</term><term>Chaperons moléculaires</term><term>Facteurs de virulence des Bordetella</term><term>Membrane cellulaire</term><term>Protéines du choc thermique</term><term>Protéines périplasmiques</term><term>Serine endopeptidases</term><term>Spécificité du substrat</term><term>Structure tertiaire des protéines</term><term>Transport de protéines</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The chaperone/protease DegP belongs to the HtrA superfamily and is involved in protein quality control in the periplasm of Gram-negative bacteria. In Escherichia coli, typical substrates are unfolded or misfolded globular proteins that trigger the rearrangement of inactive DegP hexamers into substrate-sequestering 12- or 24-mers 'cages' for refolding or degradation. In Bordetella pertussis, DegP(Bp) facilitates, in addition, the secretion of FHA, a long β-helical adhesin that passes through the periplasm in an extended conformation. We show that DegP(Bp) exists as soluble trimers and as a membrane-associated form. Different substrates interact differently with the distinct forms of DegP(Bp), and membrane-associated DegP(Bp) has high affinity for non-native FHA. Unlike more globular substrates, FHA does not efficiently mediate rearrangement of trimers into proteolytically active, short-lived dodecamers. In contrast to these dodecamers, membrane-associated DegP(Bp) is not committed to substrate degradation, although it is proteolytically competent. In B. pertussis, membrane-associated DegP(Bp) thus represents a specific functional form serving as a holding chaperone for client proteins including FHA. If FHA secretion is impaired, membrane-associated DegP(Bp) participates in its degradation. This form of DegP(Bp) is appropriate to handle substrates unsuitable to be sequestered in cages or non-folded, secretory proteins that must not be degraded.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Hauts-de-France</li><li>Nord-Pas-de-Calais</li></region><settlement><li>Lille</li></settlement></list><tree><noCountry><name sortKey="De Paepe, Diane" sort="De Paepe, Diane" uniqKey="De Paepe D" first="Diane" last="De Paepe">Diane De Paepe</name><name sortKey="Drobecq, Herve" sort="Drobecq, Herve" uniqKey="Drobecq H" first="Hervé" last="Drobecq">Hervé Drobecq</name><name sortKey="Gilleron, Martine" sort="Gilleron, Martine" uniqKey="Gilleron M" first="Martine" last="Gilleron">Martine Gilleron</name><name sortKey="Gutsche, Irina" sort="Gutsche, Irina" uniqKey="Gutsche I" first="Irina" last="Gutsche">Irina Gutsche</name><name sortKey="Jacob Dubuisson, Francoise" sort="Jacob Dubuisson, Francoise" uniqKey="Jacob Dubuisson F" first="Françoise" last="Jacob-Dubuisson">Françoise Jacob-Dubuisson</name><name sortKey="Jamin, Marc" sort="Jamin, Marc" uniqKey="Jamin M" first="Marc" last="Jamin">Marc Jamin</name><name sortKey="Locht, Camille" sort="Locht, Camille" uniqKey="Locht C" first="Camille" last="Locht">Camille Locht</name><name sortKey="Willery, Eve" sort="Willery, Eve" uniqKey="Willery E" first="Eve" last="Willery">Eve Willery</name></noCountry><country name="France"><region name="Hauts-de-France"><name sortKey="Baud, Catherine" sort="Baud, Catherine" uniqKey="Baud C" first="Catherine" last="Baud">Catherine Baud</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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